This project attempts to study the nature of protein aggregation that occurs due to heat denaturation and the presence of chemical denaturants. Light scattering results showed that bovine pancreatic RNase A aggregated at elevated temperature at pH 7. We are now interested in the relationship between the occurrence of aggregation and the change in tertiary and secondary structures of RNase A. Both CD and calorimetry measurements will be carried out to qualitatively and quantitatively explain the aggregation process.